ID   PEPB_STRA5              Reviewed;         601 AA.
AC   Q8E0C9;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Group B oligopeptidase PepB;
DE            EC=3.4.24.-;
GN   Name=pepB; OrderedLocusNames=SAG0805;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA   Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA   Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA   Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA   Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
CC   -!- FUNCTION: Has oligopeptidase activity and degrades a variety of small
CC       bioactive peptides, including bradykinin, neurotensin, and peptide
CC       fragments of substance P and adrenocorticotropin. Also hydrolyzes the
CC       synthetic collagen-like substrate N-(3-[2-furyl]acryloyl)-Leu-Gly-Pro-
CC       Ala (FALGPA).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the peptidase M3 family. {ECO:0000305}.
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DR   EMBL; AE009948; AAM99692.1; -; Genomic_DNA.
DR   RefSeq; NP_687820.1; NC_004116.1.
DR   RefSeq; WP_001282902.1; NC_004116.1.
DR   AlphaFoldDB; Q8E0C9; -.
DR   SMR; Q8E0C9; -.
DR   STRING; 208435.SAG0805; -.
DR   MEROPS; M03.007; -.
DR   EnsemblBacteria; AAM99692; AAM99692; SAG0805.
DR   KEGG; sag:SAG0805; -.
DR   PATRIC; fig|208435.3.peg.811; -.
DR   HOGENOM; CLU_021290_2_0_9; -.
DR   OMA; YRQTMFA; -.
DR   Proteomes; UP000000821; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1370.20; -; 1.
DR   InterPro; IPR013647; OligopepF_N_dom.
DR   InterPro; IPR042088; OligoPept_F_C.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR004438; Peptidase_M3B.
DR   PANTHER; PTHR11804; PTHR11804; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   Pfam; PF08439; Peptidase_M3_N; 1.
DR   TIGRFAMs; TIGR00181; pepF; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Zinc.
FT   CHAIN           1..601
FT                   /note="Group B oligopeptidase PepB"
FT                   /id="PRO_0000078171"
FT   ACT_SITE        387
FT                   /evidence="ECO:0000250"
FT   BINDING         386
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         390
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         393
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   601 AA;  69605 MW;  5FB0C326468695CE CRC64;
     MSDNRSHIEE KYQWDLTTVF ATDELWETEV VELTQAIDNA KGFSGHLLDS SQSLLEITEV
     ELDLSRRLEK VYVYASMKND QDTTVAKYQE FQAKATALYA KFSETFSFYE PELLQLSESD
     YQSFLLEMPD LQKYDHFFEK IFANKPHVLS QNEEELLAGA SEIFGAAGET FEILDNADMV
     FPVVKNAKGE EVELTHGNFI SLMESSDRTV RKEAYQAMYS TYEQFQHTYA KTLQTNVKSQ
     NFKARVHHYQ SARQSALSAN FIPEEVYETL IKTVNHHLPL LHRYMKLRQK VLGLDDLKMY
     DVYTPLSQMD MSFTYDEALK KSEEVLAIFG EAYSERVHRA FTERWIDVHV NKGKRSGAYS
     GGSYDTNAFM LLNWQDTLDN LYTLVHETGH SLHSTFTREN QPYVYGDYSI FLAEIASTTN
     ENILTETLLK EVKDDKNRFA ILNHYLDGFK GTIFRQTQFA EFEHAIHVAD QEGQVLTSEY
     LNNLYAELNE KYYGLTKEDN HFIQYEWARI PHFYYNYYVF QYATGFAAAN YLAERIVNGN
     PEDKEAYLNY LKAGNSDYPL NVIAKAGVDM TSADYLDAAF RVFEERLVEL ENLVAKGVHN
     D